LYS_BPCP1
ID LYS_BPCP1 Reviewed; 339 AA.
AC P15057; Q38009;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 29-SEP-2021, entry version 136.
DE RecName: Full=Lysozyme;
DE EC=3.2.1.17;
DE AltName: Full=CP-1 lysin;
DE AltName: Full=Endolysin;
DE AltName: Full=Muramidase;
GN Name=CPL1; Synonyms=22;
OS Streptococcus phage Cp-1 (Bacteriophage Cp-1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Cepunavirus.
OX NCBI_TaxID=10747;
OH NCBI_TaxID=1313; Streptococcus pneumoniae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3422470; DOI=10.1073/pnas.85.3.914;
RA Garcia E., Garcia J.L., Garcia P., Arraras A., Sanchez-Puelles J.M.,
RA Lopez R.;
RT "Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its
RT bacteriophages.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:914-918(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8648702; DOI=10.1128/jvi.70.6.3678-3687.1996;
RA Martin A.C., Lopez R., Garcia P.;
RT "Analysis of the complete nucleotide sequence and functional organization
RT of the genome of Streptococcus pneumoniae bacteriophage Cp-1.";
RL J. Virol. 70:3678-3687(1996).
RN [3]
RP MUTAGENESIS OF ASP-10 AND GLU-37.
RX PubMed=1390634; DOI=10.1021/bi00151a016;
RA Sanz J.M., Garcia P., Garcia J.L.;
RT "Role of Asp-9 and Glu-36 in the active site of the pneumococcal CPL1
RT lysozyme: an evolutionary perspective of lysozyme mechanism.";
RL Biochemistry 31:8495-8499(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH
RP CHOLINE, AND MUTAGENESIS OF ASP-92; GLU-94 AND ASP-182.
RX PubMed=14527392; DOI=10.1016/j.str.2003.09.005;
RA Hermoso J.A., Monterroso B., Albert A., Galan B., Ahrazem O., Garcia P.,
RA Martinez-Ripoll M., Garcia J.L., Menendez M.;
RT "Structural basis for selective recognition of pneumococcal cell wall by
RT modular endolysin from phage Cp-1.";
RL Structure 11:1239-1249(2003).
CC -!- FUNCTION: Responsible for the separation of the host daughter cells at
CC the end of cell division and participates in the liberation of progeny
CC bacteriophage into the medium. Strictly depends on the presence of
CC choline-containing cell walls for activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17;
CC -!- INTERACTION:
CC P15057; P67413: udk; Xeno; NbExp=2; IntAct=EBI-11615908, EBI-11615933;
CC -!- DOMAIN: The C-terminal domain comprising the repeats is involved in
CC choline binding.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}.
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DR EMBL; J03586; AAA32204.1; -; Genomic_DNA.
DR EMBL; Z47794; CAA87744.1; -; Genomic_DNA.
DR PIR; A31086; MUBPCP.
DR RefSeq; NP_044837.1; NC_001825.1.
DR PDB; 1H09; X-ray; 2.10 A; A=2-339.
DR PDB; 1OBA; X-ray; 2.45 A; A=1-339.
DR PDB; 2IXU; X-ray; 2.28 A; A=1-339.
DR PDB; 2IXV; X-ray; 1.96 A; A=1-339.
DR PDB; 2J8F; X-ray; 1.84 A; A=1-339.
DR PDB; 2J8G; X-ray; 1.69 A; A=1-339.
DR PDBsum; 1H09; -.
DR PDBsum; 1OBA; -.
DR PDBsum; 2IXU; -.
DR PDBsum; 2IXV; -.
DR PDBsum; 2J8F; -.
DR PDBsum; 2J8G; -.
DR SMR; P15057; -.
DR IntAct; P15057; 1.
DR CAZy; GH25; Glycoside Hydrolase Family 25.
DR GeneID; 1261221; -.
DR KEGG; vg:1261221; -.
DR EvolutionaryTrace; P15057; -.
DR PRO; PR:P15057; -.
DR Proteomes; UP000009089; Genome.
DR GO; GO:0003796; F:lysozyme activity; IDA:CACAO.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:CACAO.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR008270; Glyco_hydro_25_AS.
DR InterPro; IPR018077; Glyco_hydro_fam25_subgr.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01473; Choline_bind_1; 2.
DR Pfam; PF19127; Choline_bind_3; 1.
DR Pfam; PF01183; Glyco_hydro_25; 1.
DR SMART; SM00641; Glyco_25; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51170; CW; 5.
DR PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1.
DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase;
KW Reference proteome; Repeat.
FT CHAIN 1..339
FT /note="Lysozyme"
FT /id="PRO_0000208259"
FT DOMAIN 5..206
FT /note="Ch-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT REPEAT 200..219
FT /note="Cell wall-binding 1"
FT REPEAT 220..239
FT /note="Cell wall-binding 2"
FT REPEAT 241..260
FT /note="Cell wall-binding 3"
FT REPEAT 261..280
FT /note="Cell wall-binding 4"
FT REPEAT 281..300
FT /note="Cell wall-binding 5"
FT REPEAT 303..322
FT /note="Cell wall-binding 6"
FT ACT_SITE 10
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT MUTAGEN 10
FT /note="D->A,E,H,K,N: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:1390634"
FT MUTAGEN 37
FT /note="E->A: 95% loss of activity."
FT /evidence="ECO:0000269|PubMed:1390634"
FT MUTAGEN 37
FT /note="E->D: 63% loss of activity."
FT /evidence="ECO:0000269|PubMed:1390634"
FT MUTAGEN 37
FT /note="E->K: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:1390634"
FT MUTAGEN 37
FT /note="E->Q: 13% loss of activity."
FT /evidence="ECO:0000269|PubMed:1390634"
FT MUTAGEN 92
FT /note="D->A: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:14527392"
FT MUTAGEN 94
FT /note="E->A,Q: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:14527392"
FT MUTAGEN 182
FT /note="D->A: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:14527392"
FT CONFLICT 44
FT /note="P -> R (in Ref. 2; AAA32204)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2J8G"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2J8G"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:2J8G"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2J8G"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:2J8G"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2J8G"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2J8G"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:2J8G"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2J8G"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:2J8G"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:2J8G"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:1H09"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:2J8G"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:2J8G"
SQ SEQUENCE 339 AA; 39190 MW; E2947566AC676B05 CRC64;
MVKKNDLFVD VSSHNGYDIT GILEQMGTTN TIIKISESTT YLNPCLSAQV EQSNPIGFYH
FARFGGDVAE AEREAQFFLD NVPMQVKYLV LDYEDDPSGD AQANTNACLR FMQMIADAGY
KPIYYSYKPF THDNVDYQQI LAQFPNSLWI AGYGLNDGTA NFEYFPSMDG IRWWQYSSNP
FDKNIVLLDD EEDDKPKTAG TWKQDSKGWW FRRNNGSFPY NKWEKIGGVW YYFDSKGYCL
TSEWLKDNEK WYYLKDNGAM ATGWVLVGSE WYYMDDSGAM VTGWVKYKNN WYYMTNERGN
MVSNEFIKSG KGWYFMNTNG ELADNPSFTK EPDGLITVA
